X-ray-diffraction studies of fibrils formed from peptide fragments of transthyretin

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Two synthetic peptide fragments of the plasma protein transthyretin (TTR), previously shown to form fibrillar structures in vitro, have been examined using electron microscopy and X-ray diffraction. The fibrils displayed all characteristics of cross β-sheet conformation with antiparallel strand spacing of 4.7 Å and intersheet spacings of 8 - 10 Å as well as reflections indicating further lateral repeating units. A third peptide containing a substitution equivalent to a mutation in TTR known to increase the propensity of TTR to form amyloid was also examined. It also formed fibrils and showed similar cross β-sheet structure, but with closer intersheet packing than its native equivalent.

Original languageEnglish
Pages (from-to)991-998
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - 14 May 1993

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